GenomeNet

Database: UniProt
Entry: A0A1G4QU05_9CAUL
LinkDB: A0A1G4QU05_9CAUL
Original site: A0A1G4QU05_9CAUL 
ID   A0A1G4QU05_9CAUL        Unreviewed;       498 AA.
AC   A0A1G4QU05;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:SCW47907.1};
GN   ORFNames=SAMN02927928_1513 {ECO:0000313|EMBL:SCW47907.1};
OS   Asticcacaulis taihuensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Asticcacaulis.
OX   NCBI_TaxID=260084 {ECO:0000313|EMBL:SCW47907.1, ECO:0000313|Proteomes:UP000199150};
RN   [1] {ECO:0000313|EMBL:SCW47907.1, ECO:0000313|Proteomes:UP000199150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3431 {ECO:0000313|EMBL:SCW47907.1,
RC   ECO:0000313|Proteomes:UP000199150};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000256|ARBA:ARBA00002974}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000720};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FMTS01000001; SCW47907.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G4QU05; -.
DR   STRING; 260084.SAMN02927928_1513; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000199150; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF61; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT   DOMAIN          13..399
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        133
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         343
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   498 AA;  56080 MW;  646F4FC21A56DBE2 CRC64;
     MSEQAPKCPF HQTTTAGAPV VDNQNSLTAG PRGPVLLQDY QLIEKLAHQN RERIPERVVH
     AKGWGAHGTF TVTHDITRYT RAALFARVGK QTPLITRFST VAGELGAADA ERDVRGFSVK
     FYTEEGNWDL VGNNTPVFFI RDPYKFPDFI HTQKRHPKTH LRSPTAMWDY WSLSPEALHQ
     VTILMSDRGI PVSPMHMNGY GSHTYSFINA VNERFWVKFH FKPHKGKVNL TNEEAAKLIG
     KTRESYQEAL FGAIEAGDFP RWDLFVQVMP ELEAETTLYN PFDLTKVWPH GDYPLIPVGV
     MELNRNPDNY FNEVEQAAYS PSNIVPGIGF SPDKVLQARI FSYADAHRYR LGTHYEALPV
     NAPKCPVNTY HADGQMRFFA QFGGNPDAYY EPNSFGGPKE APEYREPPLK ISGDADRYNH
     RDGNDDYSQP RALFNLFSDG EKQRTCASIA GSMKGVPQFI IERALTHFDR IDPAYGAGIR
     KALAHGGDAE VQATRSLD
//
DBGET integrated database retrieval system